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Biomolecules Flashcards

1
Q

What are the types of carbohydrate?

A
  1. Monosaccharides
  2. Disaccharides
  3. Polysaccharides
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2
Q

Fructose + Glucose = ?

A

Sucrose + H20

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3
Q

Galactose + Glucose = ?

A

Lactose + H20

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4
Q

Glucose + Glucose = ?

A

Maltose + H20

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5
Q

What are the biological roles of carbohydrate?

A
  1. Primary source of energy for cells
  2. Anticoagulant
  3. Antigen
  4. Hormones
  5. Framework of the body
  6. Backup energy source
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6
Q

What are the properties of monosaccharides?

A
  1. Crystalline
  2. Sweet
  3. soluble in water
  4. easy to digest
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7
Q

What are the properties of disaccharides?

A
  1. Crystalline
  2. Sweet
  3. soluble in water
  4. must breakdown into monosaccharides before digesting
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8
Q

What are homopolysaccharides?

A

homopolysaccharides are polysaccharides that are made of the same monosaccharides

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9
Q

What are heteropolysaccharides?

A

heteropolysaccharides are polysaccharides that are made of different types of monosaccharides

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10
Q

What bond is used to link monosaccharides together?

A

glycosidic bond

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11
Q

What is the polysaccharide found in insects?

A

Chitin

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12
Q

What is the polysaccharide found in plants?

A

Starch and cellulose

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13
Q

What is the polysaccharide found in animals?

A

Glycogen

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14
Q

What are the properties of polysaccharides?

A
  1. do not form crystals
  2. not sweet
  3. insoluble in water
  4. not osmotically active
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15
Q

What are the 3 hormones that regulate glycogen?

A
  1. Insulin
  2. Glucagon
  3. Epinephrine
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16
Q

How is insulin made?

A

Made of protein containing 51 amino acids secreted by beta cells in the pancreas when blood glucose is high

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17
Q

What is the effect of insulin?

A

Insulin stimulates glycogen synthesis

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18
Q

How is glucagon made?

A

Made up of protein containing 29 amino acids secreted by alpha cells in pancreas when blood glucose level is low.

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19
Q

What is the effect of glucagon?

A

glucagon stimulates glycogen degradation

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20
Q

How is Epinephrine/Adrenaline made?

A
  • Produced by adrenal glands located on top of kidneys

- Derivative of amino acid tyrosine

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21
Q

What is the effect of Epinephrine/Adrenaline?

A

Binds to cell surface receptors (e.g. in liver), activates the adenylate cyclase signaling pathway and stimulates glycogen degradation

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22
Q

What are the biological roles of lipids?

A
  1. Form cell membranes around our cells
  2. Act as energy stores and are broken down to generate ATP
  3. Hormones
  4. Vitamins
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23
Q

What is the composition of a phospholipid?

A

1 glycerol + 2 fatty acid chains (hydrophobic tail) + 1 phosphate group (hydrophilic head)

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24
Q

Is LOW density lipoprotein (LDL) good or bad cholesterol?

A

Bad cholesterol

25
Q

Is HIGH density lipoprotein (HDL) good or bad cholesterol?

A

Good cholesterol

26
Q

What is the composition of Triglycerides?

A

3 fatty acids + 1glycerol

27
Q

Where is Triglycerides stored?

A

adipose cells (fat cells)

28
Q

Is Triglycerides soluble in water?

A

Triglycerides is not solube in water

29
Q

How is Triglycerides transported?

A

Transported by lipoproteins.

30
Q

What is fatty acids?

A

It is the building blocks of lipids

31
Q

what are the properties of saturated fatty acids?

A
  1. No double C-C bond
  2. Molecules are more straight
  3. Solid at room temperature
32
Q

What are the properties of unsaturated fatty acids?

A
  1. contains double C-C bond
  2. Causes bends in molecules
  3. Liquid at room temperature
33
Q

Why is steroids classified as a lipid?

A

because their non-polar and hydrophobic nature

34
Q

What is the role of steroids?

A

They are chemical messengers - most hormones are steroids

35
Q

What is the distinguish feature of the molecular structure of steroids?

A

6 carbon and 5 carbond rings

36
Q

What is protein?

A

It is the building block of the body

37
Q

What are the roles of protein?

A
  • enzymes
  • involved in muscle contraction (actin/myosin in muscle)
  • involved in production of antibodies (protect us from diseases)
  • hormones (Insulin)
  • involved in transportation (e.g. hemoglobin)
  • involved in support (collagen, keratin…)
38
Q

What bond is used to link amino acid?

A

peptide bonds

39
Q

How many amino acids are there?

40
Q

What are the 3 main categories of amino acid?

A
  1. Non polar “hydrophobic” nine in total.
  2. Uncharged polar, six in total.
  3. Charged polar, five in total.
41
Q

What are the characteristics of amino acids?

A
  1. Amino acids are “Ampholytes” - They can act as either an acid or a base.
  2. They are “Zwitterions” - molecules that have both a positive and a negative charge.
  3. Because of their ionic nature they have extremely high melting temperatures.
42
Q

What are peptides?

A

more than 1 amino acid linked by peptide bonds

43
Q

What are the 4 types of structure of protein?

A
  1. Primary
  2. Secondary
  3. Tertiary
  4. Quarternary
44
Q

What is the primary structure?

A

linear sequence of amino acids joined together by a peptide bond

45
Q

What is secondary structure?

A

folding of primary structure caused by hydrogen bonds.

46
Q

what is alpha helix?

A

Helical arrangement of amino acids in the polypeptide chain which is maintained by hydrogen bonds parallel to the helix axis.

47
Q

What is beta sheets?

A

Hydrogen bonds form between adjacent sections of polypeptides that are either running in the same direction (parallel) or in the opposite direction (anti-parallel).

48
Q

What is beta - turns?

A

reverse the direction of the polypeptide chain and are often found connecting the ends of anti-parallel b-pleated sheets.

49
Q

What is tertiary structure?

A

Three-dimensional arrangement of the amino acids in the polypeptide chain.
It is biologically active.

50
Q

What is quarternary structure?

A

Protein composed of more than one polypeptide chain in a spatial arrangement.
Tertiary strutures interacting with one another form quarternary structure.

51
Q

What are the different classes of protein?

A

Enzymes: Accelerate biochemical reactions

Structural: Form biological structures

Transport: Carry biochemically important substances

Defense: Protect the body from foreign invaders

Globular: Complex folds, irregularly shaped tertiary structures

Fibrous: Extended, simple folds – generally structural proteins

Membrane: In direct physical contact with a membrane; generally water insoluble.

Soluble: Water soluble; can be anywhere in the cell.

52
Q

What is an enzyme?

A

Biological catalyst that control a reaction without being changed itself

53
Q

What is the role of enzyme?

A
  1. converts substrate into product

2. lower the activation energy, so a reaction proceeds at a much faster rate

54
Q

How does enzyme work?

A

substrate enters the active site of the enzyme and transforms it into a product.

active site site and substrate have complementary shapes, enabling them to bind together with a high degree of specificity

55
Q

What are the 2 hypothesis of how enzyme binds to substrate?

A
  1. Lock and key model

2. Induced fit model.

56
Q

What are the environmental factors that affect enzyme structure and activity?

A
  1. Heat (temperature) disrupts hydrogen bonding and other forces that stabilise protein structure, causing the enzyme to change its shape and lose activity.
  2. pH changes alter the charge of the amino acids of a protein, thus affecting the structure and ability to bind a substrate.
57
Q

what are the types of nucleic acid?

A
  1. Deoxyribonucleic acid (DNA)
  2. Ribonucleic acid (RNA)
    - mRNA (messenger)
    - tRNA (transfer)
    - rRNA (ribosomal)
58
Q

What is DNA made of?

A
  1. Sugars
  2. Phosphates
  3. Nucleotide bases:
    - Adenine (A)
    - Thymine (T)
    - Cytosine (C)
    - Guanine (G)
59
Q

What is the central dogma of molecular biology?

A
  1. Replication
  2. Transcription (DNA to RNA)
  3. Translation ( RNA to protein)

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